UniProt functional annotation for Q16543



	UniProt functional annotation for Q16543

UniProt code: Q16543.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (PubMed:8666233). Inhibits HSP90AA1 ATPase activity (PubMed:23569206). {ECO:0000269|PubMed:23569206, ECO:0000269|PubMed:8666233}.

Subunit: Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (PubMed:29127155). Forms a complex with Hsp90/HSP90AB1 and CDK6 (PubMed:9482106). Interacts with HSP90AA1 (PubMed:23569206, PubMed:27353360). Interacts with AR, CDK4, CDK6 and EIF2AK1 (PubMed:11036079, PubMed:11085988, PubMed:9150368, PubMed:9482106). Interacts with RB1 (By similarity). Interacts with KSR1 (PubMed:10409742). Interacts with FLCN, FNIP1 and FNIP2 (PubMed:27353360). {ECO:0000250|UniProtKB:Q63692, ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:11036079, ECO:0000269|PubMed:11085988, ECO:0000269|PubMed:23569206, ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155, ECO:0000269|PubMed:9150368, ECO:0000269|PubMed:9482106}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:9482106}.

Ptm: Constitutively sumoylated by UBE2I. {ECO:0000269|PubMed:17709345}.

Similarity: Belongs to the CDC37 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (PubMed:8666233). Inhibits HSP90AA1 ATPase activity (PubMed:23569206). {ECO:0000269\|PubMed:23569206, ECO:0000269\|PubMed:8666233}.


Subunit:		Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (PubMed:29127155). Forms a complex with Hsp90/HSP90AB1 and CDK6 (PubMed:9482106). Interacts with HSP90AA1 (PubMed:23569206, PubMed:27353360). Interacts with AR, CDK4, CDK6 and EIF2AK1 (PubMed:11036079, PubMed:11085988, PubMed:9150368, PubMed:9482106). Interacts with RB1 (By similarity). Interacts with KSR1 (PubMed:10409742). Interacts with FLCN, FNIP1 and FNIP2 (PubMed:27353360). {ECO:0000250\|UniProtKB:Q63692, ECO:0000269\|PubMed:10409742, ECO:0000269\|PubMed:11036079, ECO:0000269\|PubMed:11085988, ECO:0000269\|PubMed:23569206, ECO:0000269\|PubMed:27353360, ECO:0000269\|PubMed:29127155, ECO:0000269\|PubMed:9150368, ECO:0000269\|PubMed:9482106}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:9482106}.
Ptm:		Constitutively sumoylated by UBE2I. {ECO:0000269\|PubMed:17709345}.
Similarity:		Belongs to the CDC37 family. {ECO:0000305}.